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Literature summary for 2.7.11.21 extracted from

  • Park, C.H.; Park, J.E.; Kim, T.S.; Kang, Y.H.; Soung, N.K.; Zhou, M.; Kim, N.H.; Bang, J.K.; Lee, K.S.
    Mammalian polo-like kinase 1 (Plk1) promotes proper chromosome segregation by phosphorylating and delocalizing the PBIP1-CENP-Q complex from kinetochores (2015), J. Biol. Chem., 290, 8569-8581.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of HA-tagged wild-type and K82M mutant enzymes in Spodoptera frugiperda Sf9 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
K82M a kinase-inactive mutant Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
kinetochore
-
Homo sapiens 776
-
nucleus
-
Homo sapiens 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + CENP-Q Homo sapiens
-
ADP + phosphorylated CENP-Q
-
?
ATP + PBIP1 Homo sapiens Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism ADP + phosphorylated PBIP1
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NYY3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant HA-tagged wild-type and K82M mutant enzymes from Spodoptera frugiperda Sf9 cells Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + CENP-Q
-
Homo sapiens ADP + phosphorylated CENP-Q
-
?
ATP + CENP-Q phosphorylation of nine CENP-Q residues Thr123, Thr135, Ser138, Ser139, Ser248, Ser249, Ser253, Ser255, and Thr256, clustered in two regions, mutation of all nine residues to Ala completely eliminated Plk1-dependent CENP-Q phosphorylation in vitro Homo sapiens ADP + phosphorylated CENP-Q
-
?
ATP + PBIP1 Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism Homo sapiens ADP + phosphorylated PBIP1
-
?

Synonyms

Synonyms Comment Organism
Plk1
-
Homo sapiens
Polo-like kinase 1
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens

General Information

General Information Comment Organism
malfunction a failure in Plk1 regulation of the timing of CENP-Q dissociation from kinetochores leads to chromosome missegregation. Inhibition of Plk1 activity greatly diminishes hyperphosphorylates, slow-migrating PBIP1 (but not the moderately phosphorylated PBIP1 forms because of the presence of Plk1-independent phosphorylation) and appears to eliminate slow-migrating CENP-Q forms Homo sapiens
metabolism cell cycle-dependent regulation of the PBIP1-CENP-Q complex involving the enzyme, overview Homo sapiens
physiological function Plk1 is a protein kinase that localizes to subcellular structures called kinetochores to promote mitotic progression. Plk1 interacts with and regulates a kinetochore-associated PBIP1-CENP-Q complex. This is a tightly regulated, cell cycle-dependent process, the deregulation of which leads to improper chromosome segregation and mitotic progression. The event is likely critical for maintaining genomic integrity and preventing aneuploidy. PBIP1 and CENP-Q are ubiquitinated in a manner that does not require Plk1. Plk1 dissociates CENP-Q from chromatin without disrupting the PBIP1-CENP-Q complex. Plk1-dependent CENP-Q phosphorylation negatively regulates the ability of the PBIP1-CENP-Q complex to associate with chromatin. Plk1 regulates the timing of CENP-Q dissociation from kinetochores. Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism and then phosphorylates the CENP-Q subunit of the PBIP1-CENP-Q complex Homo sapiens